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rdf:type |
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lifeskim:mentions |
umls-concept:C0003069,
umls-concept:C0018787,
umls-concept:C0043457,
umls-concept:C0181904,
umls-concept:C0392747,
umls-concept:C0596235,
umls-concept:C0596972,
umls-concept:C0597484,
umls-concept:C0597717,
umls-concept:C0728873,
umls-concept:C1167622,
umls-concept:C1514562,
umls-concept:C1521743,
umls-concept:C1621574,
umls-concept:C1704646,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
2
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pubmed:dateCreated |
2008-8-7
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pubmed:abstractText |
The Na(+)/Ca(2+) exchanger is the major Ca(2+) extrusion mechanism in cardiac myocytes. The activity of the cardiac Na(+)/Ca(2+) exchanger is dynamically regulated by intracellular Ca(2+). Previous studies indicate that Ca(2+) binding to a high-affinity Ca(2+)-binding domain (CBD1) in the large intracellular loop is involved in regulation. We generated transgenic zebrafish with cardiac-specific expression of CBD1 linked to yellow and cyan fluorescent protein. Ca(2+) binding to CBD1 induces conformational changes, as detected by fluorescence resonance energy transfer. With this transgenic fish model, we were able to monitor conformational changes of the Ca(2+) regulatory domain of Na(+)/Ca(2+) exchanger in intact hearts. Treatment with the positive inotropic agents ouabain and isoproterenol increased both Ca(2+) transients and Ca(2+)-induced changes in fluorescence resonance energy transfer. The results indicate that Ca(2+) regulation of the Na(+)/Ca(2+) exchanger domain CBD1 changes with inotropic state. The transgenic fish models will be useful to further characterize the regulatory properties of the Na(+)/Ca(2+) exchanger in vivo.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-10425730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-10571531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-11029397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-11158165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-11967535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-12095866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-12664089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-1484286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-15298897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-16110506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-16179590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-16600866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-16774926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-17166939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-17962412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-2549177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-6736024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-7769381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-8077237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-8295934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18550703-8831145
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caffeine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Isoproterenol,
http://linkedlifedata.com/resource/pubmed/chemical/Nifedipine,
http://linkedlifedata.com/resource/pubmed/chemical/Ouabain,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Calcium Exchanger,
http://linkedlifedata.com/resource/pubmed/chemical/Tnnt2 protein, zebrafish,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin T,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0363-6143
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
295
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C388-93
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:18550703-Animals,
pubmed-meshheading:18550703-Animals, Genetically Modified,
pubmed-meshheading:18550703-Caffeine,
pubmed-meshheading:18550703-Calcium Signaling,
pubmed-meshheading:18550703-DNA, Antisense,
pubmed-meshheading:18550703-Dogs,
pubmed-meshheading:18550703-Embryo, Nonmammalian,
pubmed-meshheading:18550703-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:18550703-Heart,
pubmed-meshheading:18550703-Isoproterenol,
pubmed-meshheading:18550703-Myocardial Contraction,
pubmed-meshheading:18550703-Nifedipine,
pubmed-meshheading:18550703-Ouabain,
pubmed-meshheading:18550703-Peptide Fragments,
pubmed-meshheading:18550703-Protein Conformation,
pubmed-meshheading:18550703-Protein Structure, Tertiary,
pubmed-meshheading:18550703-Sodium-Calcium Exchanger,
pubmed-meshheading:18550703-Troponin T,
pubmed-meshheading:18550703-Zebrafish,
pubmed-meshheading:18550703-Zebrafish Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Conformational changes of a Ca2+-binding domain of the Na+/Ca2+ exchanger monitored by FRET in transgenic zebrafish heart.
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pubmed:affiliation |
Department of Physiology, Cardiovascular Research Laboratories, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095-1760, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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